| dc.contributor.author | Fatahiya, Mohamed Tap | |
| dc.contributor.author | Ameera, Ishak | |
| dc.contributor.author | Ragheed, Hussam | |
| dc.contributor.author | Nurul Bahiyah, Ahmad Khairudin | |
| dc.date.accessioned | 2012-09-05T13:28:15Z | |
| dc.date.available | 2012-09-05T13:28:15Z | |
| dc.date.issued | 2012-02-27 | |
| dc.identifier.citation | p. 123-128 | en_US |
| dc.identifier.isbn | 978-145771989-9 | |
| dc.identifier.uri | http://ezproxy.unimap.edu.my:2080/stamp/stamp.jsp?tp=&arnumber=6178968 | |
| dc.identifier.uri | http://dspace.unimap.edu.my/123456789/20839 | |
| dc.description | Link to publisher's homepage at http://ieeexplore.ieee.org/ | en_US |
| dc.description.abstract | The structure and trajectories of the 41–56 β-hairpins
from the protein G (PDB ID: 1GB1) has been studied using
Molecular Dynamics (MD) simulation. The purpose of this
project is to investigate the pathway of the folding process. The
simulation was run at 325 K for 50ns. The linear chain of the
protein sequence became completely folded to β-hairpin structure
at nearly 40ns. There were 18 interactions of hydrogen Bonds
involved in the model. The model was aligned to the Nuclear
Magnetic Resonance (NMR) structure with the RMSD value of
3.05 Å for overall structure and 1.04 Å for the turning part. The
values of RMSD showed the comparison of the model and the
native structure. | en_US |
| dc.language.iso | en | en_US |
| dc.publisher | Institute of Electrical and Electronics Engineers (IEEE) | en_US |
| dc.relation.ispartofseries | Proceedings of the International Conference on Biomedical Engineering (ICoBE 2012) | en_US |
| dc.subject | Molecular Dynamics (MD) | en_US |
| dc.subject | Protein folding | en_US |
| dc.subject | Protein G | en_US |
| dc.title | Molecular dynamics folding simulation of β-hairpins from protein G | en_US |
| dc.type | Working Paper | en_US |
| dc.contributor.url | fatahiyamohdtap@yahoo.com | en_US |
| dc.contributor.url | nurulbahiyah@ic.utm.my | en_US |
